A cold-active esterase of Streptomyces coelicolor A3(2): from genome sequence to enzyme activity
IR@CSIR-IIIM
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Title |
A cold-active esterase of Streptomyces coelicolor A3(2): from genome sequence to enzyme activity
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Creator |
Soror, Sameh H.
Verma, V. Rao, Ren Rasool, Shafaq Koul, S. Qazi, G. N. Cullum, John |
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Subject |
Biological Sciences
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Description |
The genome sequence of Streptomyces coelicolor A3(2) contains 51 putative lipase and esterase genes mostly of unknown function. The gene estB (locus SCO 6966) was expressed as a His-tagged protein in E. coli. Esterase B was active at low temperatures exerting its maximum activity at 30°C and retaining more than 25% of its activity at 4°C. The optimum pH was 8–8.5. The enzyme was active against short synthetic p-nitrophenylesters (C2–C10) with maximum activity towards the acetate ester (C2). The esterase was tested on 13 series of racemic esters of potential interest for the synthesis of chiral pharmaceutical compounds. 4 of the series were substrates and a modestdegree of enantioselectivity was observed (enantiomeric ratios of 1.1–1.9). |
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Date |
2007
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Type |
Article
PeerReviewed |
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Format |
application/pdf
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Identifier |
http://iiim.csircentral.net/183/1/10.1007s10295-007-0224-6.pdf
Soror, Sameh H. and Verma, V. and Rao, Ren and Rasool, Shafaq and Koul, S. and Qazi, G. N. and Cullum, John (2007) A cold-active esterase of Streptomyces coelicolor A3(2): from genome sequence to enzyme activity. Journal of Industrial Microbiology & Biotechnology, 34 (8). pp. 525-531. ISSN 1367-5435 |
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Relation |
http://dx.doi.org/10.1007/s10295-007-0224-6
http://iiim.csircentral.net/183/ |
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